Benjamin Lau
@bennilau.bsky.social
.. interested in fundamental questions of RNA-protein biology. EIPOD PostDoc @EMBL, Duss and Mahamid Group
December 11, 2025 at 7:00 PM
With the GPATCH1-DHX35 and TFIP11-DHX15 pairs present, our work opens intriguing questions regarding splicing fidelity. Special thanks to Reinhard Lührmann for guiding us ribosome folks!
February 28, 2025 at 6:09 AM
With the GPATCH1-DHX35 and TFIP11-DHX15 pairs present, our work opens intriguing questions regarding splicing fidelity. Special thanks to Reinhard Lührmann for guiding us ribosome folks!
Known to regulate splicing of pre-mRNAs with non-canonical splice sites, we provide fiery structural details into the action of GPATCH1-DHX35. Soni et al. reported similar insights from S. Pombe, suggesting a conserved route to mitigate a common source of error during splicing. rdcu.be/ebDtT
Structures of aberrant spliceosome intermediates on their way to disassembly
Nature Structural & Molecular Biology - Here, the authors provide insights into a splicing quality control mechanism. The Gpl1–Gih35 complex binds to the active site of aberrant...
rdcu.be
February 28, 2025 at 6:09 AM
Known to regulate splicing of pre-mRNAs with non-canonical splice sites, we provide fiery structural details into the action of GPATCH1-DHX35. Soni et al. reported similar insights from S. Pombe, suggesting a conserved route to mitigate a common source of error during splicing. rdcu.be/ebDtT
We identify catalytically active spliceosomes that were intercepted by quality control: they contain a suboptimal pre-mRNA that is recognized by the G-patch protein GPATCH1, which binds its cognate RNA helicase DHX35, while disassembly factors DHX15-TFIP11-GCFC2 bind nearby.
February 28, 2025 at 6:09 AM
We identify catalytically active spliceosomes that were intercepted by quality control: they contain a suboptimal pre-mRNA that is recognized by the G-patch protein GPATCH1, which binds its cognate RNA helicase DHX35, while disassembly factors DHX15-TFIP11-GCFC2 bind nearby.
Splicing in C.t. is surprisingly similar to humans (expanding @hitenmadhani.bsky.social work to thermophiles): CryoEM structures of 𝑐𝑡spliceosomes with a core resolution of 2.2A (one of the best in the field🔥) are similar to recently published ones by the Plaschka and Cochella Labs rdcu.be/ebDt7
February 28, 2025 at 6:09 AM
Splicing in C.t. is surprisingly similar to humans (expanding @hitenmadhani.bsky.social work to thermophiles): CryoEM structures of 𝑐𝑡spliceosomes with a core resolution of 2.2A (one of the best in the field🔥) are similar to recently published ones by the Plaschka and Cochella Labs rdcu.be/ebDt7